Background
Caprine skin is a promising biomaterial for tissue‐engineering applications. However, tissue processing is required before its xenogenic use.
Aims
Therefore, the purpose of this study was to evaluate the structural integrity and biocompatibility of the caprine skin after de‐epithelialization, using sodium chloride (NaCl) and trypsin solutions, followed by de‐cellularization using sodium dodecyl sulfate (SDS) solution.
Materials & Methods
The caprine skin was de‐epithelialized using NaCl (2‐4 mol/L) and trypsin (0.25%‐0.5%) followed by the treatment of SDS (1%‐4%) solution over a period of time. Acellularity of the prepared matrix was confirmed histologically and characterized by appropriate staining, scanning electron microscopy (SEM), DNA quantification, and Fourier‐transform infrared (FTIR) spectroscopy. The caprine acellular dermal matrix (CADM) was used for the repair of spontaneously occurring abdominal hernia in ten buffaloes. The biocompatibility of the CADM was evaluated using clinical, hematological, biochemical, and anti‐oxidant parameters.
Results
Histologically, the skin treated with 0.25% trypsin in 4 mol/L NaCl for 8 hours resulted in complete de‐epithelialization. Further treatment with 2% SDS for 48 hours demonstrated complete acellularity and orderly arranged collagen fibers. The SEM confirmed a preservation of collagen arrangement within CADM. The DNA content was significantly (P < .05) lower in CADM (46.20 ± 7.94 ng/mg) as compared to fresh skin (662.56 ± 156.11 ng/mg) indicating effective acellularity. The FTIR spectra showed characteristic collagen peaks of amide A, amide B, amide I, amide II, and amide III in CADM. All the 10 animals recovered uneventfully and remained sound. Hematological, biochemical, and anti‐oxidants findings were unremarkable.
Conclusion
Results indicated the acceptance and biocompatibility of the xenogenic caprine acellular dermal matrix for abdominal hernia repair in buffaloes without complications.
Treatment with 2% SDS for 48 h results in 92.54% reduction in DNA contents and complete acellularity of the bubaline diaphragm.• FTIR spectrum of decellularized diaphragm has shown all characteristic transmittance peaks of the collagen.• Bubaline diaphragm matrix shows excellent repair efficiency and biocompatibility for abdominal hernia repair in cattle without complications.• Insert a highlight no longer than 85 characters. HIGHLIGHTS 2 Vora, S.D.; et al.
Animal tissues are extensively used as scaffolds for tissue engineering and regenerative therapies. They are typically subjected to decellularization process to obtain a cell-free extracellular matrix (ECM) scaffolds. It is important to identify chemical structure of the ECM scaffolds and Fourier transform infrared (FTIR) appears to be a technique of choice. In this chapter, FTIR spectra of native and decellularized buffalo aortae, buffalo diaphragms, goat skin, and native bovine cortical bone are presented. The transmittance peaks are that of organic collagen amide A, amide B, amide I, amide II and amide III chemical functional groups in both native and decellularized aortae, diaphragms and skin. In bone, the transmittance peaks are that of inorganic ν1, ν3 PO43−, OH− in addition to organic collagen amide A, amide B, amide I, amide II and amide III chemical functional groups. These important transmittance peaks of the tissue samples will help researchers in defining the chemical structure of these animal tissues.
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